Structural basis for LAR-RPTP/Slitrk complex-mediated synaptic adhesion (Q27696175)

1

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Kee Hun Kim

2

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Yeonsoo Choi

4

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Doyoun Kim

5

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Cha Yeon Kim

6

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Soo Jin Kim

7

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Minhye Kim

8

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Ji Seung Ko

9

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Seong-Gyu Lee

10

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Gayoung Choii

11

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Jungyong Nam

12

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Won Do Heo

13

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Eunjoon Kim

14

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Jie-Oh Lee

15

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Jaewon Ko

16

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Ho Min Kim

Neuroligins and neurexins link synaptic function to cognitive disease

17

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language of work or name

English

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publication date

14 November 2014

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published in

Nature Communications

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volume

5

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page(s)

5423

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LAR-RPTPs: synaptic adhesion molecules that shape synapse development

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Molecular characterization of the human transmembrane protein-tyrosine phosphatase delta. Evidence for tissue-specific expression of alternative human transmembrane protein-tyrosine phosphatase delta isoforms

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The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1

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IL-1 receptor accessory protein-like 1 associated with mental retardation and autism mediates synapse formation by trans-synaptic interaction with protein tyrosine phosphatase δ

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Interleukin-1 receptor accessory protein organizes neuronal synaptogenesis as a cell adhesion molecule

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Postsynaptic TrkC and presynaptic PTPσ function as a bidirectional excitatory synaptic organizing complex.

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Slitrks control excitatory and inhibitory synapse formation with LAR receptor protein tyrosine phosphatases

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Selective control of inhibitory synapse development by Slitrk3-PTPδ trans-synaptic interaction.

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Identification and characterization of Slitrk, a novel neuronal transmembrane protein family controlling neurite outgrowth

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Slitrks as emerging candidate genes involved in neuropsychiatric disorders

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Trans-synaptic adhesions between netrin-G ligand-3 (NGL-3) and receptor tyrosine phosphatases LAR, protein-tyrosine phosphatase delta (PTPdelta), and PTPsigma via specific domains regulate excitatory synapse formation

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The leucine-rich repeat as a protein recognition motif

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Proteoglycan-Specific Molecular Switch for RPTP Clustering and Neuronal Extension

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Structure and evolution of neurexin genes: insight into the mechanism of alternative splicing

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SAM68 regulates neuronal activity-dependent alternative splicing of neurexin-1

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A structural basis for antigen recognition by the T cell-like lymphocytes of sea lamprey

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Structural insights into the Slit-Robo complex

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Neurexin mediates the assembly of presynaptic terminals

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Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin

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The Immunoglobulin-like Domains 1 and 2 of the Protein Tyrosine Phosphatase LAR Adopt an Unusual Horseshoe-like Conformation

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Crystal structure of the tandem phosphatase domains of RPTP LAR

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Splice Form Dependence of β-Neurexin/Neuroligin Binding Interactions

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Cartography of neurexin alternative splicing mapped by single-molecule long-read mRNA sequencing

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An extracellular interactome of immunoglobulin and LRR proteins reveals receptor-ligand networks.

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Functional significance of the LAR receptor protein tyrosine phosphatase family in development and diseases

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Lateral assembly of the immunoglobulin protein SynCAM 1 controls its adhesive function and instructs synapse formation.

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Combinatorial homophilic interaction between gamma-protocadherin multimers greatly expands the molecular diversity of cell adhesion

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LRRTM2 functions as a neurexin ligand in promoting excitatory synapse formation

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Neuroligin-1 performs neurexin-dependent and neurexin-independent functions in synapse validation

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SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses

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Calsyntenins function as synaptogenic adhesion molecules in concert with neurexins

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LAR receptor protein tyrosine phosphatases in the development and maintenance of excitatory synapses

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inferred from DOI database lookup

7 January 2021

based on heuristic

Visualizing proteins and macromolecular complexes by negative stain EM: from grid preparation to image acquisition.

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS6423

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NCOMMS6423

1 reference

Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

ADS bibcode

2014NatCo...5.5423U

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1050198375

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1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

25394468

1 reference

Consolidated OpenCitations Corpus – April 2017